Biotechnology & Genetic Engineering Reviews: Volume 26 by Stephen E. Harding

By Stephen E. Harding

Containing more than a dozen original, significant evaluation articles from authors released in prime journals and covering very important advancements in commercial, agricultural, and clinical purposes of biotechnology, this latest version from the well-established hardcover overview sequence focuses totally on the genetic manipulation of organisms. protecting concerns starting from gene expression and genetic laws to plant bioreactors and enzymatic processing, this reference will profit scholars within the fields of biochemistry, genetics, molecular biology, and pharmaceutical sciences.

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2006). Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minor. Nature Biotechnology 24, 1591-97. W. et al. (2000). Differential mitogen-activated protein kinase stimulation by Fc gamma receptor IIa and Fc gamma receptor IIIb determines the activation phenotype of human neutrophils. Journal of Immunology 164, 6530-37. Cremata, J. A, Sorell, L. and Montesino, R. (2003). Hypogalactosylation of serum IgG in patients with coeliac disease. Clinical and Experimental Immunology 133, 422-29.

And Gasmi, L. (1997). Activation of human neutrophils by soluble immune complexes: role of Fc gamma RII and Fc gamma RIIIb in stimulation of the respiratory burst and elevation of intracellular Ca2+. Annals of the New York Academy of Sciences 832, 341-57. Famm, K. and Winter, G. (2006). Engineering aggregation-resistant proteins by directed evolution. Protein Engineering Design and Selection 19, 479-81. Farooq. , et al. (1997). Glycosylation of polyclonal and paraprotein IgG in multiple myeloma.

2007) Interestingly, the bacterial and viral IgG binding protein share overlapping interaction sites on IgG-Fc, namely the inter-CH2/CH3 domain region. This is also the region of the molecule that expresses the interaction site for FcRn; therefore, when engineering IgG-Fc to modulate interactions with FcRn, and influence catabolic half-life, the consequent impact on binding other ligands should be taken into account. Antibody production in non-mammalian systems It will be evident that an ability to produce selected homogenous glycoforms of recombinant antibody molecules could be advantageous.

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